Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/248666
Share/Export:
logo share SHARE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

The behavior of sea anemone actinoporins at the water-membrane interface

AuthorsGarcía-Ortega, Lucía; Alegre-Cebollada, Jorge; García-Linares, S.; Bruix, M. CSIC ORCID; Martínez-del-Pozo, Álvaro; Gavilanes, José G.
KeywordsActinoporin
Equinatoxin
Sticholysin
Membrane-pore
Pore-forming-toxin
Issue Date20-May-2011
PublisherElsevier BV
CitationBiochimica et Biophysica Acta - Biomembranes 1808: 2275-2288 (2011)
AbstractActinoporins constitute a group of small and basic α-pore forming toxins produced by sea anemones. They display high sequence identity and appear as multigene families. They show a singular behaviour at the water-membrane interface: In aqueous solution, actinoporins remain stably folded but, upon interaction with lipid bilayers, become integral membrane structures. These membranes contain sphingomyelin, display phase coexistence, or both. The water soluble structures of the actinoporins equinatoxin II (EqtII) and sticholysin II (StnII) are known in detail. The crystalline structure of a fragaceatoxin C (FraC) nonamer has been also determined. The three proteins fold as a β-sandwich motif flanked by two α-helices, one of them at the N-terminal end. Four regions seem to be especially important: A cluster of aromatic residues, a phosphocholine binding site, an array of basic amino acids, and the N-terminal α-helix. Initial binding of the soluble monomers to the membrane is accomplished by the cluster of aromatic amino acids, the array of basic residues, and the phosphocholine binding site. Then, the N-terminal α-helix detaches from the β-sandwich, extends, and lies parallel to the membrane. Simultaneously, oligomerization occurs. Finally, the extended N-terminal α-helix penetrates the membrane to build a toroidal pore. This model has been however recently challenged by the cryo-EM reconstruction of FraC bound to phospholipid vesicles. Actinoporins structural fold appears across all eukaryotic kingdoms in other functionally unrelated proteins. Many of these proteins neither bind to lipid membranes nor induce cell lysis. Finally, studies focusing on the therapeutic potential of actinoporins also abound. © 2011 Elsevier B.V. All rights reserved.
Description14 pags, 9 figs
Publisher version (URL)http://dx.doi.org/10.1016/j.bbamem.2011.05.012
URIhttp://hdl.handle.net/10261/248666
Identifiersdoi: 10.1016/j.bbamem.2011.05.012
issn: 0005-2736
Appears in Collections:(IQFR) Artículos

Files in This Item:
File Description SizeFormat
behavior_sea_anemone_actinoporins.pdf2,56 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work

Google ScholarTM

Check


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.